Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin
Hydroxytyrosol (HT), one of the main phenolic components of olive oil, has attracted considerable interest for its biological properties, including a remarkable antioxidant and anti-inflammatory power and, recently, for its ability to interfere with the amyloid aggregation underlying several human d...
| Main Authors: | , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2020-06-01
|
| Series: | International Journal of Molecular Sciences |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1422-0067/21/13/4636 |
| _version_ | 1797563812954505216 |
|---|---|
| author | Ivana Sirangelo Margherita Borriello Silvia Vilasi Clara Iannuzzi |
| author_facet | Ivana Sirangelo Margherita Borriello Silvia Vilasi Clara Iannuzzi |
| author_sort | Ivana Sirangelo |
| collection | DOAJ |
| description | Hydroxytyrosol (HT), one of the main phenolic components of olive oil, has attracted considerable interest for its biological properties, including a remarkable antioxidant and anti-inflammatory power and, recently, for its ability to interfere with the amyloid aggregation underlying several human diseases. We report here a broad biophysical approach and cell biology techniques that allowed us to characterize the molecular mechanisms by which HT affects insulin amyloid aggregation and the related cytotoxicity. Our data show that HT is able to fully inhibit insulin amyloid aggregation and this property seems to be ascribed to the stabilization of the insulin monomeric state. Moreover, HT completely reverses the toxic effect produced by amyloid insulin aggregates in neuroblastoma cell lines by fully inhibiting the production of toxic amyloid species. These findings suggest that the beneficial effects of olive oil polyphenols, including HT, may arise from multifunctional activities and suggest possible a application of this natural compound in the prevention or treatment of amyloid-associated diseases. |
| first_indexed | 2024-03-10T18:48:27Z |
| format | Article |
| id | doaj.art-7cd89f99ea574b89afe9fbb87be3e88a |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T18:48:27Z |
| publishDate | 2020-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-7cd89f99ea574b89afe9fbb87be3e88a2023-11-20T05:21:53ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-06-012113463610.3390/ijms21134636Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human InsulinIvana Sirangelo0Margherita Borriello1Silvia Vilasi2Clara Iannuzzi3Department of Precision Medicine, Università degli Studi della Campania “Luigi Vanvitelli”, Via L. De Crecchio 7, 80138 Naples, ItalyDepartment of Precision Medicine, Università degli Studi della Campania “Luigi Vanvitelli”, Via L. De Crecchio 7, 80138 Naples, ItalyInstitute of Biophysics, National Research Council, Via Ugo La Malfa, 153, 90146 Palermo, ItalyDepartment of Precision Medicine, Università degli Studi della Campania “Luigi Vanvitelli”, Via L. De Crecchio 7, 80138 Naples, ItalyHydroxytyrosol (HT), one of the main phenolic components of olive oil, has attracted considerable interest for its biological properties, including a remarkable antioxidant and anti-inflammatory power and, recently, for its ability to interfere with the amyloid aggregation underlying several human diseases. We report here a broad biophysical approach and cell biology techniques that allowed us to characterize the molecular mechanisms by which HT affects insulin amyloid aggregation and the related cytotoxicity. Our data show that HT is able to fully inhibit insulin amyloid aggregation and this property seems to be ascribed to the stabilization of the insulin monomeric state. Moreover, HT completely reverses the toxic effect produced by amyloid insulin aggregates in neuroblastoma cell lines by fully inhibiting the production of toxic amyloid species. These findings suggest that the beneficial effects of olive oil polyphenols, including HT, may arise from multifunctional activities and suggest possible a application of this natural compound in the prevention or treatment of amyloid-associated diseases.https://www.mdpi.com/1422-0067/21/13/4636amyloid aggregationhuman insulinhydroxytyrosolamyloid toxicity |
| spellingShingle | Ivana Sirangelo Margherita Borriello Silvia Vilasi Clara Iannuzzi Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin International Journal of Molecular Sciences amyloid aggregation human insulin hydroxytyrosol amyloid toxicity |
| title | Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin |
| title_full | Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin |
| title_fullStr | Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin |
| title_full_unstemmed | Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin |
| title_short | Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin |
| title_sort | hydroxytyrosol inhibits protein oligomerization and amyloid aggregation in human insulin |
| topic | amyloid aggregation human insulin hydroxytyrosol amyloid toxicity |
| url | https://www.mdpi.com/1422-0067/21/13/4636 |
| work_keys_str_mv | AT ivanasirangelo hydroxytyrosolinhibitsproteinoligomerizationandamyloidaggregationinhumaninsulin AT margheritaborriello hydroxytyrosolinhibitsproteinoligomerizationandamyloidaggregationinhumaninsulin AT silviavilasi hydroxytyrosolinhibitsproteinoligomerizationandamyloidaggregationinhumaninsulin AT claraiannuzzi hydroxytyrosolinhibitsproteinoligomerizationandamyloidaggregationinhumaninsulin |